title: Chaperone role for proteins p618 and p892 in the extracellular tail development of Acidianus two-tailed virus.
abstract: The crenarchaeal Acidianus two-tailed virus (ATV) undergoes a remarkable morphological development, extracellularly and independently of host cells, by growing long tails at each end of a spindle-shaped virus particle. Initial work suggested that an intermediate filament-like protein, p800, is involved in this process. We propose that an additional chaperone system is required, consisting of a MoxR-type AAA ATPase (p618) and a von Willebrand domain A (VWA)-containing cochaperone, p892. Both proteins are absent from the other known bicaudavirus, STSV1, which develops a single tail intracellularly. p618 exhibits ATPase activity and forms a hexameric ring complex that closely resembles the oligomeric complex of the MoxR-like protein RavA (YieN). ATV proteins p387, p653, p800, and p892 interact with p618, and with the exception of p800, all bind to DNA. A model is proposed to rationalize the interactions observed between the different protein and DNA components and to explain their possible structural and functional roles in extracellular tail development.
authors.affiliation: Archaea Centre, Department of Biology, University of Copenhagen, DK-2200 Copenhagen N, Denmark. uscheele@bio.ku.dk
authors.forename: Urte
authors.initials: U
authors.lastname: Scheele
authors.forename: Susanne
authors.initials: S
authors.lastname: Erdmann
authors.forename: Ernst J
authors.initials: EJ
authors.lastname: Ungewickell
authors.forename: Catarina
authors.initials: C
authors.lastname: Felisberto-Rodrigues
authors.forename: Miguel
authors.initials: M
authors.lastname: Ortiz-Lombardía
authors.forename: Roger A
authors.initials: RA
authors.lastname: Garrett
mesh_terms: D041541:Acidianus / Q000821:virology*; D000251:Adenosine Triphosphatases / Q000378:metabolism; D000595:Amino Acid Sequence; D004267:DNA Viruses / Q000502:physiology* / Q000648:ultrastructure; D004279:DNA, Viral / Q000378:metabolism; D018832:Molecular Chaperones / Q000378:metabolism*; D008969:Molecular Sequence Data; D025941:Protein Interaction Mapping; D016415:Sequence Alignment; D014764:Viral Proteins / Q000378:metabolism*; D014771:Virion / Q000502:physiology / Q000648:ultrastructure
chemical_list: D004279:DNA, Viral; D018832:Molecular Chaperones; D014764:Viral Proteins; D000251:Adenosine Triphosphatases